about
Poly-small ubiquitin-like modifier (PolySUMO)-binding proteins identified through a string searchHECT and RING finger families of E3 ubiquitin ligases at a glanceRING-type E3 ligases: master manipulators of E2 ubiquitin-conjugating enzymes and ubiquitinationFeedback regulation of cholesterol uptake by the LXR-IDOL-LDLR axisStructure of a RING E3 ligase and ubiquitin-loaded E2 primed for catalysisMechanism of ubiquitylation by dimeric RING ligase RNF4Multivalent interactions of the SUMO-interaction motifs in RING finger protein 4 determine the specificity for chains of the SUMOStructural insight into SUMO chain recognition and manipulation by the ubiquitin ligase RNF4Structural analysis of poly-SUMO chain recognition by the RNF4-SIMs domainA C2HC zinc finger is essential for the RING-E2 interaction of the ubiquitin ligase RNF125A single heterologously expressed plant cellulose synthase isoform is sufficient for cellulose microfibril formation in vitro.Exploring the RING-catalyzed ubiquitin transfer mechanism by MD and QM/MM calculations.An arginine-rich motif of ring finger protein 4 (RNF4) oversees the recruitment and degradation of the phosphorylated and SUMOylated Krüppel-associated box domain-associated protein 1 (KAP1)/TRIM28 protein during genotoxic stress.Multiple Arkadia/RNF111 structures coordinate its Polycomb body association and transcriptional control.Dimeric switch of Hakai-truncated monomers during substrate recognition: insights from solution studies and NMR structureMechanism of cullin3 E3 ubiquitin ligase dimerization.Contribution of E3-ubiquitin ligase activity to HIV-1 restriction by TRIM5alpha(rh): structure of the RING domain of TRIM5alpha.Fission yeast Dma1 requires RING domain dimerization for its ubiquitin ligase activity and mitotic checkpoint function.STUbLs in chromatin and genome stability.Trafficking of the transcription factor Nrf2 to promyelocytic leukemia-nuclear bodies: implications for degradation of NRF2 in the nucleusA SUMO-targeted ubiquitin ligase is involved in the degradation of the nuclear pool of the SUMO E3 ligase Siz1.The FA Core Complex Contains a Homo-dimeric Catalytic Module for the Symmetric Mono-ubiquitination of FANCI-FANCD2.IAPS and ubiquitylation.Decoding the SUMO signal.Specificity and disease in the ubiquitin systemSUMO chain-induced dimerization activates RNF4.Arkadia, a novel SUMO-targeted ubiquitin ligase involved in PML degradation.The RING-Finger Ubiquitin Ligase HAF1 Mediates Heading date 1 Degradation during Photoperiodic Flowering in Rice.Asymmetric nature of two subunits of RAD18, a RING-type ubiquitin ligase E3, in the human RAD6A-RAD18 ternary complex.Structure of the yeast Bre1 RING domain.Smac mimetics activate the E3 ligase activity of cIAP1 protein by promoting RING domain dimerization.MPSR1 is a cytoplasmic PQC E3 ligase for eliminating emergent misfolded proteins in Arabidopsis thaliana.The Molecular Interface Between the SUMO and Ubiquitin Systems.
P2860
Q24301465-19D95B9D-B0BC-4D85-B95B-89230A98A536Q24599672-78A1415B-B011-4282-9775-5D3DB95C8105Q26850008-FAF252AB-E068-42C1-AB85-B57227D7A8F7Q27026250-4CE56582-1C8B-4E18-BEDF-3FFB820B1D43Q27670947-4FB1EF05-CCB1-44CF-8640-641D6C0F9834Q27671855-6BAA857F-513A-46FE-9A15-AA6D2E84BFA4Q27680434-F1AA1AFF-0CE6-47D5-9826-EE0A3D9DD108Q27684476-305B3A24-2767-429E-A5A3-3E6D9E22B0C4Q27690266-D95F8503-A042-4800-9D6A-453D8873CD77Q28596587-3CF0DCA1-2822-41FB-8AD0-9A6F8EB8E224Q30275889-D65DF36F-F4FE-4E48-A1F3-81594451BF02Q33864109-BC94351B-022A-418C-A164-A4579E76DE03Q33947105-CFC24476-1F9B-4803-8588-A95ABFD69E15Q34056507-1FFD28A5-1DD2-41C9-9CCD-3A1B2A2DC96BQ34170693-252FD82F-536D-459E-BFAB-863CEDC08631Q34387857-6918FA66-1C3A-4A61-A4CB-3B74C5F86286Q35192942-6163DE69-9B78-403A-B91B-0E9DEF647B05Q36122076-FD4B3278-F1A5-4446-9E61-A55D42C50FF8Q36426331-8EFF7B9C-73ED-47D0-B224-EC19A9D30E17Q36850393-DA5410E5-BB1E-4F5E-9528-0896F0C0B28DQ37416477-0E486116-8EE9-4A99-B6AF-A4902FE151ABQ37607318-D7771EC2-AF42-4AA0-9288-7C5151C5003FQ37987881-57328C89-BE25-490C-87FD-72F05C15A2E5Q38091465-6534ECEC-93D9-4EFB-A3E2-6FDF80499624Q38728113-460F37FB-73B7-46CD-B64E-8D37BA005F7AQ38823924-93E80F24-AFA9-4A16-9BEC-07AD285B1864Q39175550-A51C60BA-FA88-4B3C-8191-58B686AE943CQ40618287-0B4E57A8-7B3B-4590-B2BD-080118FC3BA4Q40898008-A8FB72DC-94B8-4946-A51C-8D64214D1974Q41087270-3B196843-2DBB-4712-8FE6-15B49A101C04Q41905427-6890B881-EB9B-4A67-A062-F5C78219E992Q47102731-B7BE4E7A-0B7D-46BC-B38D-7A2A550A34F6Q51137606-66A4E645-DBF8-4328-A1FD-FCA6D3922B8B
P2860
description
2010 nî lūn-bûn
@nan
2010 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
RING domain dimerization is essential for RNF4 function
@ast
RING domain dimerization is essential for RNF4 function
@en
RING domain dimerization is essential for RNF4 function
@nl
type
label
RING domain dimerization is essential for RNF4 function
@ast
RING domain dimerization is essential for RNF4 function
@en
RING domain dimerization is essential for RNF4 function
@nl
prefLabel
RING domain dimerization is essential for RNF4 function
@ast
RING domain dimerization is essential for RNF4 function
@en
RING domain dimerization is essential for RNF4 function
@nl
P2093
P2860
P3181
P356
P1433
P1476
RING domain dimerization is essential for RNF4 function
@en
P2093
Chu Wai Liew
Huaiyu Sun
Tony Hunter
P2860
P3181
P356
10.1042/BJ20100957
P407
P577
2010-10-01T00:00:00Z